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Beatriz Martínez - One of the best experts on this subject based on the ideXlab platform.
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a novel bacteriocin produced by lactobacillus plantarum lpu4 as a valuable candidate for biopreservation in artisanal raw milk cheese
Dairy Science & Technology, 2015Co-Authors: C Milioni, Beatriz Martínez, Sara Deglinnocenti, Barbara Turchi, Filippo Fratini, Domenico Cerri, Roberto FischettiAbstract:Indigenous lactic acid bacteria-producing bacteriocins could enhance the microbiological safety of traditional cheeses. This study aimed to detect bacteriocinogenic strains among 35 Lactobacillus plantarum isolated from artisanal, raw sheep-milk cheeses. The isolates were identified by API 50 CHL and species-specific PCR. As displayed by agar well-diffusion assay, the cell-free supernatant of L. plantarum LpU4 showed the highest antimicrobial activity against Enterococcus faecalis JH2-2. The activity was not detected after treatment with proteinase K, pepsine and pronase. An active peptide band was shown by tricine–sodium dodecyl sulfate (SDS)–polyacrylamide gel electrophoresis and subsequent bioassay. MALDI-TOF analysis revealed a protein of 4,866.7 Da, having no homology with other known bacteriocins. The novel bacteriocin (named plantaricin LpU4) was heat stable (121 °C for 15 min), unaffected by chemicals as Tween 20, SDS, Triton ×100, EDTA, NaCl and exposure to a wide range of pH. The synthetic machinery encoding for the plantaricin was plasmid-located, as deduced by plasmids curing. Activity spectrum included several lactic acid bacteria and Staphylococcus aureus strains having antibiotic resistance phenotype. Plantaricin LpU4 showed a bacteriostatic mode of action and an enhanced activity at acidic pHs. Maximal production (3,200 AU.mL−1) was reached during the late exponential phase of growth of L. plantarum LpU4. Relatively low temperature (15–25 °C) and initial pH between 5.5 and 6.2 increased the production. Since L. plantarum LpU4 produced the bacteriocin under experimental conditions mimicking the cheese environment, it could be considered a promising candidate for use as biopreservative in traditional cheese.
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influence of ca 2 ions on the activity of lantibiotics containing a mersacidin like lipid ii binding motif
Applied and Environmental Microbiology, 2009Co-Authors: Tim Böttiger, Beatriz Martínez, Tanja Schneider, Hansgeorg Sahl, Imke WiedemannAbstract:Mersacidin binds to lipid II and thus blocks the transglycosylation step of the cell wall biosynthesis. Binding of lipid II involves a special motif, the so-called mersacidin-lipid II binding motif, which is conserved in a major subgroup of lantibiotics. We analyzed the role of Ca(2+) ions in the mode of action of mersacidin and some related peptides containing a mersacidin-like lipid II binding motif. We found that the stimulating effect of Ca(2+) ions on the antimicrobial activity known for mersacidin also applies to plantaricin C and lacticin 3147. Ca(2+) ions appear to facilitate the interaction of the lantibiotics with the bacterial membrane and with lipid II rather than being an essential part of a peptide-lipid II complex. In the case of lacticin 481, both the interaction with lipid II and the antimicrobial activity were Ca(2+) independent.
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Influence of Ca2+ Ions on the Activity of Lantibiotics Containing a Mersacidin-Like Lipid II Binding Motif
Applied and Environmental Microbiology, 2009Co-Authors: Tim Böttiger, Tanja Schneider, Beatriz MartínezAbstract:Mersacidin binds to lipid II and thus blocks the transglycosylation step of the cell wall biosynthesis. Binding of lipid II involves a special motif, the so-called mersacidin-lipid II binding motif, which is conserved in a major subgroup of lantibiotics. We analyzed the role of Ca2+ ions in the mode of action of mersacidin and some related peptides containing a mersacidin-like lipid II binding motif. We found that the stimulating effect of Ca2+ ions on the antimicrobial activity known for mersacidin also applies to plantaricin C and lacticin 3147. Ca2+ ions appear to facilitate the interaction of the lantibiotics with the bacterial membrane and with lipid II rather than being an essential part of a peptide-lipid II complex. In the case of lacticin 481, both the interaction with lipid II and the antimicrobial activity were Ca2+ independent.
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Lipid II-Based Antimicrobial Activity of the Lantibiotic Plantaricin C
Applied and Environmental Microbiology, 2006Co-Authors: Tim Böttiger, Raquel Regina Bonelli, Tanja Schneider, Beatriz MartínezAbstract:We analyzed the mode of action of the lantibiotic plantaricin C (PlnC), produced by Lactobacillus plantarum LL441. Compared to the well-characterized type A lantibiotic nisin and type B lantibiotic mersacidin, which are both able to interact with the cell wall precursor lipid II, PlnC displays structural features of both prototypes. In this regard, we found that lipid II plays a key role in the antimicrobial activity of PlnC besides that of pore formation. The pore forming activity of PlnC in whole cells was prevented by shielding lipid II on the cell surface. However, in contrast to nisin, PlnC was not able to permeabilize Lactococcus lactis cells or to form pores in 1,2-dioleoyl-sn-glycero-3-phosphocholine liposomes supplemented with 0.1 mol% purified lipid II. This emphasized the different requirements of these lantibiotics for pore formation. Using cell wall synthesis assays, we identified PlnC as a potent inhibitor of (i) lipid II synthesis and (ii) the FemX reaction, i.e., the addition of the first Gly to the pentapeptide side chain of lipid II. As revealed by thin-layer chromatography, both reactions were clearly blocked by the formation of a PlnC-lipid I and/or PlnC-lipid II complex. On the basis of the in vivo and in vitro activities of PlnC shown in this study and the structural lipid II binding motifs described for other lantibiotics, the specific interaction of PlnC with lipid II is discussed.
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consequences of the development of nisin resistant listeria monocytogenes in fermented dairy products
Journal of Food Protection, 2005Co-Authors: Beatriz Martínez, Diego Bravo, Ana RodriguezAbstract:Wild Listeria isolates representing serovars found in artisanal cheeses commercialized in Asturias (northern Spain) were assessed for their susceptibility to several bacteriocins. Pediocin PA-1 was the most active bacteriocin followed by enterocin AS-48, nisin, and plantaricin C. However, some Listeria monocytogenes and Listeria innocua strains were already highly resistant to PA-1. Among the wild L. monocytogenes populations, the frequency of development of nisin resistance ranged from 10(-6) up to 10(-3), depending on the strain. Highly stable mutants with increased nisin resistance (two- to fourfold) were isolated and tested for potential cross-resistance to lysozyme, EDTA, and various NaCl concentrations and pH values. All mutants were cross-resistant to lysozyme but sensitive to EDTA. In contrast, no clear correlation could be established between nisin resistance and an altered susceptibility to NaCl or pH changes. Nisin-resistant variants were able to survive and even to multiply in milk fermented by a nisin-producing Lactococcus, but the growth of the wild-type strain was inhibited. The different phenotypes evaluated in this study are indicative of the unpredictability of the consequences of the development of nisin resistance in a dairy environment. This resistance should be considered when making a risk assessment of the long-term use of nisin to control L. monocytogenes.
Michael L. Chikindas - One of the best experts on this subject based on the ideXlab platform.
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Purification, partial amino acid sequence and mode of action of pediocin PD-1, a bacteriocin produced by Pediococcus damnosus NCFB 1832
International journal of food microbiology, 2005Co-Authors: R Bauer, Michael L. ChikindasAbstract:Pediocin PD-1 is a ribosomally synthesized antimicrobial peptide produced by Pediococcus damnosus NCFB1832. It inhibits the growth of several food spoilage bacteria, including malolactic bacteria isolated from wine. Pediocin PD-1 is 2866.87F0.4 Da in size, has an isoelectric point (pI) of ca. 9.0 and, on amino acid composition, has partial homology to the lantibiotic plantaricin C. The highest activity of pediocin PD-1 against cells of Oenococcus oeni was observed at an external pH of 5.0 and at 25 8C. The primary mode of action of pediocin PD-1 is most probably due to pore formation, as indicated by the efflux of K + from metabolically active cells of O. oeni. In the presence of 10 mM gadolinium (Gd 3+ ), pediocin PD-1 did not affect cells of O. oeni. This suggests that the mode of action of pediocin PD-1 relies on a net negatively charged cell surface. In comparison to nisin, pediocin PD-1 is less active against non-growing cells of O. oeni. D 2004 Elsevier B.V. All rights reserved.
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isolation purification and partial characterization of plantaricin 423 a bacteriocin produced by lactobacillus plantarum
Journal of Applied Microbiology, 1998Co-Authors: Carol A. Reenen, L M T Dicks, Michael L. ChikindasAbstract:Lactobacillus plantarum 423, isolated from sorghum beer, produces a bacteriocin (plantaricin 423) which is inhibitory to several food spoilage bacteria and food-borne pathogens, including Bacillus cereus, Clostridium sporogenes, Enterococcus faecalis, Listeria spp. and Staphylococcus spp. Plantaricin 423 is resistant to treatment at 80 °C, but loses 50% of its activity after 60 min at 100 °C and 75% of its activity after autoclaving (121 °C, 15 min). Plantaricin 423 remains active after incubation at pH 1–10 and is inactivated when treated with pepsin, papain, α-chymotrypsin, trypsin and Proteinase K. Plantaricin 423 was partially purified and its size estimated at 3·5 kDa, as determined by tricine-SDS-PAGE. The mechanism of activity of plantaricin 423 is weakly bactericidal, as determined against Oenococcus oeni (previously Leuconostoc oenos). High DNA homology was obtained between the plasmid DNA of strain 423 and the pediocin PA-1 operon of Pediococcus acidilactici PAC 1·0, suggesting that plantaricin 423 is plasmid-encoded and related to the pediocin gene cluster.
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isolation purification and partial characterization of plantaricin 423 a bacteriocin produced by lactobacillus plantarum
Journal of Applied Microbiology, 1998Co-Authors: C A Van Reenen, Leon M. T. Dicks, Michael L. ChikindasAbstract:Lactobacillus plantarum 423, isolated from sorghum beer, produces a bacteriocin (plantaricin 423) which is inhibitory to several food spoilage bacteria and food-borne pathogens, including Bacillus cereus, Clostridium sporogenes, Enterococcus faecalis, Listeria spp. and Staphylococcus spp. Plantaricin 423 is resistant to treatment at 80 degrees C, but loses 50% of its activity after 60 min at 100 degrees C and 75% of its activity after autoclaving (121 degrees C, 15 min). Plantaricin 423 remains active after incubation at pH 1-10 and is inactivated when treated with pepsin, papain, alpha-chymotrypsin, trypsin and Proteinase K. Plantaricin 423 was partially purified and its size estimated at 3.5 kDa, as determined by tricine-SDS-PAGE. The mechanism of activity of plantaricin 423 is weakly bactericidal, as determined against Oenococcus oeni (previously Leuconostoc oenos). High DNA homology was obtained between the plasmid DNA of strain 423 and the pediocin PA-1 operon of Pediococcus acidilactici PAC 1.0, suggesting that plantaricin 423 is plasmid-encoded and related to the pediocin gene cluster.
Tim Böttiger - One of the best experts on this subject based on the ideXlab platform.
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influence of ca 2 ions on the activity of lantibiotics containing a mersacidin like lipid ii binding motif
Applied and Environmental Microbiology, 2009Co-Authors: Tim Böttiger, Beatriz Martínez, Tanja Schneider, Hansgeorg Sahl, Imke WiedemannAbstract:Mersacidin binds to lipid II and thus blocks the transglycosylation step of the cell wall biosynthesis. Binding of lipid II involves a special motif, the so-called mersacidin-lipid II binding motif, which is conserved in a major subgroup of lantibiotics. We analyzed the role of Ca(2+) ions in the mode of action of mersacidin and some related peptides containing a mersacidin-like lipid II binding motif. We found that the stimulating effect of Ca(2+) ions on the antimicrobial activity known for mersacidin also applies to plantaricin C and lacticin 3147. Ca(2+) ions appear to facilitate the interaction of the lantibiotics with the bacterial membrane and with lipid II rather than being an essential part of a peptide-lipid II complex. In the case of lacticin 481, both the interaction with lipid II and the antimicrobial activity were Ca(2+) independent.
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Influence of Ca2+ Ions on the Activity of Lantibiotics Containing a Mersacidin-Like Lipid II Binding Motif
Applied and Environmental Microbiology, 2009Co-Authors: Tim Böttiger, Tanja Schneider, Beatriz MartínezAbstract:Mersacidin binds to lipid II and thus blocks the transglycosylation step of the cell wall biosynthesis. Binding of lipid II involves a special motif, the so-called mersacidin-lipid II binding motif, which is conserved in a major subgroup of lantibiotics. We analyzed the role of Ca2+ ions in the mode of action of mersacidin and some related peptides containing a mersacidin-like lipid II binding motif. We found that the stimulating effect of Ca2+ ions on the antimicrobial activity known for mersacidin also applies to plantaricin C and lacticin 3147. Ca2+ ions appear to facilitate the interaction of the lantibiotics with the bacterial membrane and with lipid II rather than being an essential part of a peptide-lipid II complex. In the case of lacticin 481, both the interaction with lipid II and the antimicrobial activity were Ca2+ independent.
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Lipid II-Based Antimicrobial Activity of the Lantibiotic Plantaricin C
Applied and Environmental Microbiology, 2006Co-Authors: Tim Böttiger, Raquel Regina Bonelli, Tanja Schneider, Beatriz MartínezAbstract:We analyzed the mode of action of the lantibiotic plantaricin C (PlnC), produced by Lactobacillus plantarum LL441. Compared to the well-characterized type A lantibiotic nisin and type B lantibiotic mersacidin, which are both able to interact with the cell wall precursor lipid II, PlnC displays structural features of both prototypes. In this regard, we found that lipid II plays a key role in the antimicrobial activity of PlnC besides that of pore formation. The pore forming activity of PlnC in whole cells was prevented by shielding lipid II on the cell surface. However, in contrast to nisin, PlnC was not able to permeabilize Lactococcus lactis cells or to form pores in 1,2-dioleoyl-sn-glycero-3-phosphocholine liposomes supplemented with 0.1 mol% purified lipid II. This emphasized the different requirements of these lantibiotics for pore formation. Using cell wall synthesis assays, we identified PlnC as a potent inhibitor of (i) lipid II synthesis and (ii) the FemX reaction, i.e., the addition of the first Gly to the pentapeptide side chain of lipid II. As revealed by thin-layer chromatography, both reactions were clearly blocked by the formation of a PlnC-lipid I and/or PlnC-lipid II complex. On the basis of the in vivo and in vitro activities of PlnC shown in this study and the structural lipid II binding motifs described for other lantibiotics, the specific interaction of PlnC with lipid II is discussed.
Svetoslav D. Todorov - One of the best experts on this subject based on the ideXlab platform.
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Bacteriocins from Lactobacillus plantarum – production, genetic organization and mode of action
2009Co-Authors: Svetoslav D. TodorovAbstract:Bacteriocins are biologically active proteins or protein complexes that display a bactericidal mode of action towards usually closely related species. Numerous strains of bacteriocin producing Lactobacillus plantarum have been isolated in the last two decades from different ecological niches including meat, fish, fruits, vegetables, and milk and cereal products. Several of these Plantaricins have been characterized and the aminoacid sequence determined. Different aspects of the mode of action, fermentation optimization and genetic organization of the bacteriocin operon have been studied. However, numerous of bacteriocins produced by different Lactobacillus plantarum strains have not been fully characterized. In this article, a brief overview of the classification, genetics, characterization, including mode of action and production optimization for bacteriocins from Lactic Acid Bacteria in general, and where appropriate, with focus on bacteriocins produced by Lactobacillus plantarum, is presented
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Bacteriocins from Lactobacillus plantarum production, genetic organization and mode of action: produção, organização genética e modo de ação Bacteriocinas de Lactobacillus plantarum
Sociedade Brasileira de Microbiologia, 2009Co-Authors: Svetoslav D. TodorovAbstract:Bacteriocins are biologically active proteins or protein complexes that display a bactericidal mode of action towards usually closely related species. Numerous strains of bacteriocin producing Lactobacillus plantarum have been isolated in the last two decades from different ecological niches including meat, fish, fruits, vegetables, and milk and cereal products. Several of these Plantaricins have been characterized and the aminoacid sequence determined. Different aspects of the mode of action, fermentation optimization and genetic organization of the bacteriocin operon have been studied. However, numerous of bacteriocins produced by different Lactobacillus plantarum strains have not been fully characterized. In this article, a brief overview of the classification, genetics, characterization, including mode of action and production optimization for bacteriocins from Lactic Acid Bacteria in general, and where appropriate, with focus on bacteriocins produced by Lactobacillus plantarum, is presented.Bacteriocinas são proteínas ou complexos protéicos biologicamente ativos que apresentam atividade bactericida contra espécies relacionadas. Nas ultimas duas décadas, várias cepas de Lactobacillus plantarum produtoras de bacteriocinas foram isoladas de diferentes nichos ecológicos como carnes, peixes, frutas, vegetais e produtos lácteos e de cereais. Várias plantaricinas foram caracterizadas e suas seqüências de aminoácidos determinadas. Diferentes aspectos do modo de ação, otimização da fermentação e organização genética já foram estudados. Entretanto, muitas bacteriocinas produzidas por diferentes cepas de Lactobacillus plantarum ainda não foram completamente caracterizadas.Nesse artigo, apresenta-se uma breve revisão sobre a classificação, genética, caracterização, modo de ação, e otimização da produção de bacteriocinas de bactérias láticas em geral, e, quando apropriado, de bacteriocinas de Lactobacillus plantarum
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Comparison of two methods for purification of plantaricin ST31, a bacteriocin produced by Lactobacillus plantarum ST31 Comparação de dois métodos de purificação da plantaricina ST31, a bacteriocina produzida por Lactobacillus plantarum ST31
Sociedade Brasileira de Microbiologia, 2004Co-Authors: Svetoslav D. Todorov, Manuela Vaz-velho, Paul GibbsAbstract:Two methods of purification of the plantaricin ST31, a bacteriocin produced by Lactobacillus plantarum ST31 are used in this study - the method of ammonium sulfate precipitation, Sep-pack C18 cartridge and reverse-phase HPLC chromatography on C18 Nucleosil column, and the method of direct purification by cation exchange SP Sepharose Fast Flow column Amersham (Pharmacia Biotech). The purity of the products from the two experimental protocols are examined for their molecular weight, aminoacid composition and sequence. Comparison of results show that the Plantaricins purified with the two methods are identical. Both methods may be used to purify plantaricin ST31. Comparison of the yield in the purification protocols is 0.8% in the HPLC experimental protocol and 5.9% in the cation-exchange chromatography method.Dois métodos de purificação de plantaricin ST31, uma bacteriocina produzida por Lactobacillus plantarum ST31 foram usados neste estudo - o método de precipitação pelo sulfato de amônia usando cartucho Sep-pack C18 para a filtração e HPLC de fase reversa em coluna de C18 Nucleosil, e o método de purificação direta por troca catiônica SP Sepharose "Fast Flow column Amersham" (Pharmacia Biotech). A pureza dos produtos obtidos pelos dois protocolos foi examinada através da determinação dos pesos moleculares, composição e seqüência dos aminoácidos. A comparação destes resultados revelou que, em termos da pureza dos produtos, não havia diferenças entre os dois métodos de purificação podendo-se, portanto, utilizar qualquer um dos protocolos de purificação testados. No entanto, o rendimento da purificação pelo método da troca catiônica foi de 5.9% enquanto o do método HPLC foi de 0.8%
Svetoslav Dimitrov Todorov - One of the best experts on this subject based on the ideXlab platform.
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characterization of a two peptide plantaricin produced by lactobacillus plantarum mbsa4 isolated from brazilian salami
Food Control, 2016Co-Authors: Svetoslav Dimitrov Todorov, Matheus De Souza Barbosa, Iskra Ivanova, Yanath Belguesmia, Yvan Choiset, Hanitra Rabesona, Jeanmarc Chobert, Thomas HaertleAbstract:Abstract The aim of this study was to explore the biochemical and genetic features of the two-peptide bacteriocin produced by a Lactobacillus plantarum strain isolated from Italian type salami produced in Brazil ( Lb. plantarum MBSa4). Identification of bacteriocinogenic Lb. plantarum MBSa4 was performed by 16S rRNA sequencing. Expressed bacteriocin was evaluated for spectrum of activity, heat and pH stability, mechanism of action, and molecular mass. Partial purification was achieved by cation-exchange, and reversed phase - HPLC. Total DNA of Lb. plantarum MBSa4 was extracted and tested for presence of previously described bacteriocin genes. Bacteriocin MBSa4 was heat-stable, unaffected by pH 2.0 to 6.0 and active against all tested Listeria monocytogenes strains and most of tested fungi. Maximal production (1600 AU/ml) in MRS broth occurred after 22 h at 25 °C, presenting bacteriostatic activity as result of combined action of two components. The molecular mass determined by SDS-PAGE was 2.3 kDa. PCR-amplified DNA indicated the same nucleotide sequence of plantaricin W. Results indicate that Lb. plantarum MBSa4 produces plantaricin W, a two-peptide lantibiotic with remarkable anti- Listeria activity.
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Lactobacillus pentosus B231 Isolated from a Portuguese PDO Cheese: Production and Partial Characterization of Its Bacteriocin
Probiotics and Antimicrobial Proteins, 2014Co-Authors: Joana Guerreiro, Svetoslav Dimitrov Todorov, Vitor Monteiro, Carla Ramos, Bernadette Dora Gombossy Melo Franco, Rafael Chacon Ruiz Martinez, Paulo FernandesAbstract:Bacteriocin B231 produced by Lactobacillus pentosus , isolated from an artisanal raw cow’s milk protected designation of origin Portuguese cheese, is a small protein with an apparent relative mass of about 5 kDa and active against a large number of Listeria monocytogenes wild-type strains, Listeria ivanovii and Listeria innocua . Bacteriocin B231 production is highly dependent on the type of the culture media used for growth of Lact. pentosus B231. Replacement of glucose with maltose yielded the highest bacteriocin production from eight different carbon sources. Similar results were recorded in the presence of combination of glucose and maltose or galactose. Production of bacteriocin B231 reached maximal levels of 800 AU/ml during the stationary phase of growth of Lact. pentosus B231 in MRS broth at 30 °C. Bacteriocin B231 (in cell-free supernatant) was sensitive to treatment with trypsin and proteinase K, but not affected by the thermal treatment in range of 55–121 °C, or freezing (−20 °C). Bacteriocin production and inhibitory spectrum were evaluated. Gene encoding plantaricin S has been detected in the genomic DNA. Virulence potential and safety of Lact. pentosus B231 were assessed by PCR targeted the genes gel E, hy l, asa 1, esp , cyl A, efa A, ace , van A, van B, hdc 1, hdc 2, tdc and odc . The Lact. pentosus B231 strains harbored plantaricin S gene, while the occurrence of virulence, antibiotic resistance and biogenic amine genes was limited to cytolysin, hyaluronidase, aggregation substance, adhesion of collagen protein, gelatinase, tyrosine decarboxylase and vancomycin B genes.
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bacteriocins from lactobacillus plantarum production genetic organization and mode of action producao organizacao genetica e modo de acao
Brazilian Journal of Microbiology, 2009Co-Authors: Svetoslav Dimitrov TodorovAbstract:Bacteriocins are biologically active proteins or protein complexes that display a bactericidal mode of action towards usually closely related species. Numerous strains of bacteriocin producing Lactobacillus plantarum have been isolated in the last two decades from different ecological niches including meat, fish, fruits, vegetables, and milk and cereal products. Several of these Plantaricins have been characterized and the aminoacid sequence determined. Different aspects of the mode of action, fermentation optimization and genetic organization of the bacteriocin operon have been studied. However, numerous of bacteriocins produced by different Lactobacillus plantarum strains have not been fully characterized. In this article, a brief overview of the classification, genetics, characterization, including mode of action and production optimization for bacteriocins from Lactic Acid Bacteria in general, and where appropriate, with focus on bacteriocins produced by Lactobacillus plantarum, is presented.
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bacteriocins from lactobacillus plantarum production genetic organization and mode of action
Brazilian Journal of Microbiology, 2009Co-Authors: Svetoslav Dimitrov TodorovAbstract:ABSTRACT Bacteriocins are biologically active proteins or protein complexes that display a bactericidal mode of actiontowards usually closely related species. Numerous strains of bacteriocin producing Lactobacillus plantarum have been isolated in the last two decades from different ecological niches including meat, fish, fruits,vegetables, and milk and cereal products. Several of these Plantaricins have been characterized and theaminoacid sequence determined. Different aspects of the mode of action, fermentation optimization andgenetic organization of the bacteriocin operon have been studied. However, numerous of bacteriocins producedby different Lactobacillus plantarum strains have not been fully characterized. In this article, a brief overviewof the classification, genetics, characterization, including mode of action and production optimization forbacteriocins from Lactic Acid Bacteria in general, and where appropriate, with focus on bacteriocins producedby Lactobacillus plantarum , is presented.